The purpose is to elicit molecular details of conformational kinetics in polypeptides. An eventual aim is to understand the mechanisms and pathways of protein folding and denaturation-renaturation kinetics. A mathematical model of the rates for passing between the various configurational states has been established. Molecular states are determined by specification of whether each peptide unit has a helical or random coil conformation. The model has served to point out some needed experiments. Careful interpretation of experiments will yield individual peptide transition rates for a range of amino acids and permit treatment of specific proteins. Additional states will be included in a modified model in order to incorporate additional configurational forms that are observed in proteins. Many physical properties of proteins can then be calculated.